Simple and rapid separation of ortho- and paramyxovirus glycoproteins
暂无分享,去创建一个
[1] R. T. Huang. Adsorption of influenza virus to charged groups on natural and artificial surfaces , 2005, Medical Microbiology and Immunology.
[2] H. Klenk,et al. Fusion between cell membrane and liposomes containing the glycoproteins of influenza virus. , 1980, Virology.
[3] C. F. Fox,et al. Protein-protein interactions within paramyxoviruses identified by native disulfide bonding or reversible chemical cross-linking , 1980, Journal of virology.
[4] S. Udem,et al. Nature of the Sendai virus receptor: glycoprotein versus ganglioside , 1980, Journal of virology.
[5] D. Lyles. Glycoproteins of Sendai virus are transmembrane proteins. , 1979, Proceedings of the National Academy of Sciences of the United States of America.
[6] H. Klenk,et al. Association of the envelope glycoproteins of influenza virus with liposomes--a model study on viral envelope assembly. , 1979, Virology.
[7] A. Scheid,et al. Reconstitution of membranes with individual paramyxovirus glycoproteins and phospholipid in cholate solution. , 1979, Virology.
[8] H. Klenk,et al. The structure of the hemagglutinin, a determinant for the pathogenicity of influenza viruses. , 1979, Virology.
[9] J. Skehel,et al. Structure of the haemagglutinin of influenza virus. , 1979, British medical bulletin.
[10] M. Gething,et al. Purification of the fusion protein of Sendai virus: analysis of the NH2-terminal sequence generated during precursor activation. , 1978, Proceedings of the National Academy of Sciences of the United States of America.
[11] J. Skehel,et al. Evidence from studies with a cross-linking reagent that the haemagglutinin of influenza virus is a trimer. , 1977, Virology.
[12] H. Klenk,et al. Proteolytic cleavage of the viral glycoproteins and its significance for the virulence of Newcastle disease virus. , 1976, Virology.
[13] H. Klenk,et al. Activation of influenza A viruses by trypsin treatment. , 1975, Virology.
[14] P. Choppin,et al. Enhancement of the infectivity of influenza A and B viruses by proteolytic cleavage of the hemagglutinin polypeptide. , 1975, Virology.
[15] T. E. Thompson,et al. Solubilization of bacterial membrane proteins using alkyl glucosides and dioctanoyl phosphatidylcholine. , 1975, Biochimica et biophysica acta.
[16] A. Scheid,et al. Identification of biological activities of paramyxovirus glycoproteins. Activation of cell fusion, hemolysis, and infectivity of proteolytic cleavage of an inactive precursor protein of Sendai virus. , 1974, Virology.
[17] W. Schaffner,et al. A rapid, sensitive, and specific method for the determination of protein in dilute solution. , 1973, Analytical biochemistry.
[18] J. Skehel,et al. The size and shape of influenza virus neuraminidase. , 1973, Virology.
[19] M. Ohuchi,et al. Trypsin Action ontheGrowth ofSendai Virus in Tissue Culture Cells III. Structural Difference ofSendai Viruses GrowninEggsandTissue Culture Cells , 1973 .
[20] R. Rott,et al. A New Method for Purification of Myxoviruses by Zonal Centrifugation with Two Different Sucrose Density Gradients , 1972, Proceedings of the Society for Experimental Biology and Medicine. Society for Experimental Biology and Medicine.
[21] U. Hämmerling,et al. Undisturbed release of influenza virus in the presence of univalent antineuraminidase antibodies. , 1971, Virology.
[22] P. Cuatrecasas,et al. Purification of neuraminidases from Vibrio Cholerae, Clostridium Perfringens and influenza virus by affinity chromatography. , 1971, Biochemical and biophysical research communications.
[23] R. Rott,et al. Functional significance of sialidose during influenza virus multiplication. , 1966, Virology.
[24] R. Rott,et al. Isolation of a low molecular weight sialidase (neuraminidase) from influenza virus. , 1966, Biochimica et biophysica acta.
[25] R. Rott,et al. PHYSICAL AND BIOLOGICAL PROPERTIES OF INFLUENZA VIRUS COMPONENTS OBTAINED AFTER ETHER TREATMENT , 1960, The Journal of experimental medicine.
[26] O. H. Lowry,et al. Protein measurement with the Folin phenol reagent. , 1951, The Journal of biological chemistry.